ID F6CVL5_MARPP Unreviewed; 418 AA.
AC F6CVL5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Biphenyl 2,3-dioxygenase {ECO:0000313|EMBL:AEF55392.1};
DE EC=1.14.12.18 {ECO:0000313|EMBL:AEF55392.1};
GN OrderedLocusNames=Mar181_2357 {ECO:0000313|EMBL:AEF55392.1};
OS Marinomonas posidonica (strain CECT 7376 / NCIMB 14433 / IVIA-Po-181).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=491952 {ECO:0000313|EMBL:AEF55392.1, ECO:0000313|Proteomes:UP000009230};
RN [1] {ECO:0000313|EMBL:AEF55392.1, ECO:0000313|Proteomes:UP000009230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7376 / NCIMB 14433 / IVIA-Po-181
RC {ECO:0000313|Proteomes:UP000009230};
RX PubMed=23458837; DOI=10.4056/sigs.2976373;
RA Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA Detter J.C., Copeland A., Lu M., Bruce D., Detter C., Tapia R., Han S.,
RA Land M.L., Ivanova N., Mikhailova N., Johnston A.W., Sanchez-Amat A.;
RT "Complete genome sequence of Marinomonas posidonica type strain (IVIA-Po-
RT 181(T)).";
RL Stand. Genomic Sci. 7:31-43(2012).
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
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DR EMBL; CP002771; AEF55392.1; -; Genomic_DNA.
DR RefSeq; WP_013796867.1; NC_015559.1.
DR AlphaFoldDB; F6CVL5; -.
DR STRING; 491952.Mar181_2357; -.
DR KEGG; mpc:Mar181_2357; -.
DR eggNOG; COG4638; Bacteria.
DR HOGENOM; CLU_026244_4_0_6; -.
DR OrthoDB; 9769355at2; -.
DR Proteomes; UP000009230; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0018687; F:biphenyl 2,3-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR CDD; cd08880; RHO_alpha_C_ahdA1c-like; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR043264; AhdA1c-like_alpha_C.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR PANTHER; PTHR43756:SF1; 3-PHENYLPROPIONATE_CINNAMIC ACID DIOXYGENASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43756; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF00848; Ring_hydroxyl_A; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF55961; Bet v1-like; 1.
DR SUPFAM; SSF50022; ISP domain; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Dioxygenase {ECO:0000313|EMBL:AEF55392.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AEF55392.1}.
FT DOMAIN 45..131
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 418 AA; 48354 MW; A2FED05AFA6DB0D0 CRC64;
MSHENPIPMT PIWEHEDTSR IPFWAYTDKD IHKQELEKLF YKKHWCYVGL EAEIPQPGDF
KRTVIGERSV IMVRHEDNSI YVVENVCAHR GMRFCREKHG HVKSFTCPYH QWNYDLEGKL
QGVPFRRGVK QDGKAKGGMP KDFKTSDHGL TKLLVATRGG VVFASFDHDV ESFEDFLGPT
MLSYFDRMFN GRKLTLLGYN KQRIPGNWKL MQENIKDPYH PGLLHTWFVT FGLWRADNRS
ELKMDEHFRH AAMISTRGSG GKDTQTTNVS SFKESMQLND PSFLDVEVEP WWDGPTAVMM
TLFPSVILQQ QVNSVSTRHI QPNGHGSFDF VWTHFGYEDD TPDMTERRLR QANLFGPAGF
VSADDGEVIE FSQQGFEQKP FHRSLAELGG KEIEETDHMV SETLIRGMYA YWRKVMGV
//
